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X-ray structure of a protein-conducting channel

Author

Listed:
  • Bert van den Berg

    (Harvard Medical School)

  • William M. Clemons

    (Harvard Medical School)

  • Ian Collinson

    (Max Planck Institute of Biophysics)

  • Yorgo Modis

    (Children's Hospital and Harvard Medical School)

  • Enno Hartmann

    (University Luebeck, Institute for Biology)

  • Stephen C. Harrison

    (Children's Hospital and Harvard Medical School)

  • Tom A. Rapoport

    (Harvard Medical School)

Abstract

A conserved heterotrimeric membrane protein complex, the Sec61 or SecY complex, forms a protein-conducting channel, allowing polypeptides to be transferred across or integrated into membranes. We report the crystal structure of the complex from Methanococcus jannaschii at a resolution of 3.2 Å. The structure suggests that one copy of the heterotrimer serves as a functional translocation channel. The α-subunit has two linked halves, transmembrane segments 1–5 and 6–10, clamped together by the γ-subunit. A cytoplasmic funnel leading into the channel is plugged by a short helix. Plug displacement can open the channel into an ‘hourglass’ with a ring of hydrophobic residues at its constriction. This ring may form a seal around the translocating polypeptide, hindering the permeation of other molecules. The structure also suggests mechanisms for signal-sequence recognition and for the lateral exit of transmembrane segments of nascent membrane proteins into lipid, and indicates binding sites for partners that provide the driving force for translocation.

Suggested Citation

  • Bert van den Berg & William M. Clemons & Ian Collinson & Yorgo Modis & Enno Hartmann & Stephen C. Harrison & Tom A. Rapoport, 2004. "X-ray structure of a protein-conducting channel," Nature, Nature, vol. 427(6969), pages 36-44, January.
    • Handle: RePEc:nat:nature:v:427:y:2004:i:6969:d:10.1038_nature02218
    DOI: 10.1038/nature02218
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    Cited by:

    1. Alex Dajkovic & Elizabeth Hinde & Calum MacKichan & Rut Carballido-Lopez, 2016. "Dynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane," PLOS ONE, Public Library of Science, vol. 11(6), pages 1-17, June.
    2. J. Josephine Botsch & Roswitha Junker & Michèle Sorgenfrei & Patricia P. Ogger & Luca Stier & Susanne Gronau & Peter J. Murray & Markus A. Seeger & Brenda A. Schulman & Bastian Bräuning, 2024. "Doa10/MARCH6 architecture interconnects E3 ligase activity with lipid-binding transmembrane channel to regulate SQLE," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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